The disclosed devices, apparatuses, methods, assays, and processes relate generally to applying radiant electromagnetic energy to biological material, and, more particularly, relate to the application of radiant electromagnetic energy in the far-infrared (FIR) region of the electromagnetic spectrum to biological material with minimal contamination by radiation in other electromagnetic bands (such as X-rays and microwaves).
The term “far infrared” (FIR) identifies the range of the electromagnetic spectrum with free space wavelengths of about 100 to 1000 microns, or with wavenumbers from about 100 to 10 cm−1. Humans have developed extensive technology to generate and detect electromagnetic waves or vibrations throughout the electromagnetic spectrum—from the very short wavelengths and very high frequencies of gamma rays to the very long wavelengths and very low frequencies of radio waves—with the exception of the FIR gap in the spectrum existing between infrared light and millimeter wavelength microwaves. For use in the FIR gap there exists various sources and detectors, but this technology is much less well developed than the technology available for use in the other parts of the spectrum.
In the late 1980's, the research of the late Professor John Walsh at Dartmouth College and others led to the development of tunable, electron beam driven radiation sources to produce electromagnetic radiation at FIR frequencies in a flexible, tunable and affordable fashion. See U.S. Pat. No. 5,263,043 to Walsh and U.S. Pat. No. 5,790,585 to Walsh, both of which are incorporated in their entireties by this reference. This work showed that a small, compact and relatively inexpensive table top free electron laser could be a commercially practiced device to generate FIR electromagnetic waves.
Previously in the art, the common wisdom was that large biomolecules could not support vibrations, especially considering that they were always in water. Physicists thought that any possible mode of vibration would be seriously overdamped. That is to say, proteins were seen (from a mechanical point of view) more as sponges that would just go “thunk” if struck (i.e., exposed to mechanical perturbation or electromagnetic radiant energy), rather than as bells or springs which would ring or vibrate when struck. In the terminology of classical physics, it was believed that a protein structure, while having restoring forces which tend to pull the structure back towards its equilibrium conformation when the structure is forced away from its equilibrium conformation or physical shape by external forces of any nature, would not oscillate about its equilibrium conformation because the damping forces inherent in the structure and its environment would be sufficiently strong to preclude any oscillation.
However, several practitioners in the art have reported evidence that proteins are capable of vibration, even in aqueous environments. Furthermore, a number of practitioners have reported that certain proteins vibrate in the FIR band. In 1994, it was reported that the first event following impact of a visible photon on the retinal chromophore of rhodopsin was the initiation of a vibration at wavenumber 60 cm−1 (corresponding to a far infrared wavelength of about 166 microns) (Wang Q et al, “Vibrationally coherent photochemistry in the femtosecond primary event of vision,” Science, Vol. 266, 21 October 1994, p. 422). Also in 1994, researchers reported that “breathing modes” of myoglobin oscillate at FIR frequencies in association with ligand binding (binding of the oxygen which is transported by myoglobin) and that the vibrations are not overdamped (Zhu L et al, “Observation of coherent reaction dynamics in heme proteins,” Science, Vol. 266, 21 October 1994, p.629). Other experimentalists observed low frequency modes (near 20 cm−1) (Diehl M et al, “Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering,” Biophysical Journal, 1997 November; 73(5): 2726–32). Such results have generated further interest in the existence of vibrational modes in proteins, and, more particularly, vibrational modes in the FIR frequency range. Other recent work reinforces earlier findings that proteins and water can have modes in the FIR range (Xie A et al., Phys. Rev. Ltr. (2002) 88:1, 018102-1; Boyd JE et al., Phys. Rev. Ltr. (2001) 84:14, 147401-1). There are also suggestions that water associated with the KcsA potassium channel may be structured (Zhou Y et al., Nature (2001) 414:43–48).
However, no practical means exists in the art to produce and apply electromagnetic energy selectively from the FIR band to biological matter (i.e., with minimal contamination by energy from other bands, such as X-rays and microwaves). Bohr et al, in U.S. Pat. No. 6,060,293, the entire disclosure of which is incorporated herein by reference, teach methods of application of Gigahertz frequency radiation to biological matter. However, delivery of FIR radiation to biological matter requires methods and apparatus for the generation, filtering, and focusing of the FIR radiation clearly distinct from those taught by Bohr et al.
The instantly disclosed subject matter enhances the art by providing devices, apparatuses, methods, assays, and processes for delivering FIR band radiation with minimal contamination by energy in other electromagnetic bands to biological matter.